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1PKY

PYRUVATE KINASE FROM E. COLI IN THE T-STATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0009408biological_processresponse to heat
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0030955molecular_functionpotassium ion binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A1902912cellular_componentpyruvate kinase complex
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006096biological_processglycolytic process
B0009408biological_processresponse to heat
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0030955molecular_functionpotassium ion binding
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B1902912cellular_componentpyruvate kinase complex
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004743molecular_functionpyruvate kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006096biological_processglycolytic process
C0009408biological_processresponse to heat
C0016020cellular_componentmembrane
C0016301molecular_functionkinase activity
C0030955molecular_functionpotassium ion binding
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C1902912cellular_componentpyruvate kinase complex
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004743molecular_functionpyruvate kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006096biological_processglycolytic process
D0009408biological_processresponse to heat
D0016020cellular_componentmembrane
D0016301molecular_functionkinase activity
D0030955molecular_functionpotassium ion binding
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D1902912cellular_componentpyruvate kinase complex
Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IhIISKIENqEGL
ChainResidueDetails
AILE215-LEU227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30613
ChainResidueDetails
AARG32
ATHR278
BARG32
BASN34
BSER36
BASP66
BTHR67
BLYS220
BGLU222
BGLY245
BASP246
AASN34
BTHR278
CARG32
CASN34
CSER36
CASP66
CTHR67
CLYS220
CGLU222
CGLY245
CASP246
ASER36
CTHR278
DARG32
DASN34
DSER36
DASP66
DTHR67
DLYS220
DGLU222
DGLY245
DASP246
AASP66
DTHR278
ATHR67
ALYS220
AGLU222
AGLY245
AASP246

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AARG73
ALYS156
BARG73
BLYS156
CARG73
CLYS156
DARG73
DLYS156

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
ALYS220
BLYS220
CLYS220
DLYS220

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS76
ALYS319
BLYS76
BLYS319
CLYS76
CLYS319
DLYS76
DLYS319

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
ATHR278
AGLU314
ALYS220
AARG32
AARG73
ASER312

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
BTHR278
BGLU314
BLYS220
BARG32
BARG73
BSER312

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
CTHR278
CGLU314
CLYS220
CARG32
CARG73
CSER312

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
DTHR278
DGLU314
DLYS220
DARG32
DARG73
DSER312

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PDB entries from 2024-07-10

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